Thermodynamics of α- and β-structure formation in proteins

An atomic protein model with a minimalistic potential is developed and then tested on an α-helix and a β-hairpin, using exactly the same parameters for both peptides. We find that melting curves for these sequences to a good approximation can be described by a simple two-state model, with parameters that are in reasonable quantitative agreement with experimental data. Despite the apparent two-state character of the melting curves, the energy distributions are found to lack a clear bimodal shape, which is discussed in some detail. We also perform a Monte Carlo-based kinetic study and find, in accord with experimental data, that the α-helix forms faster than the β-hairpin.

@article{8c37fa54-34da-4953-a4e2-500a763807a9,
abstract = {An atomic protein model with a minimalistic potential is developed and then tested on an α-helix and a β-hairpin, using exactly the same parameters for both peptides. We find that melting curves for these sequences to a good approximation can be described by a simple two-state model, with parameters that are in reasonable quantitative agreement with experimental data. Despite the apparent two-state character of the melting curves, the energy distributions are found to lack a clear bimodal shape, which is discussed in some detail. We also perform a Monte Carlo-based kinetic study and find, in accord with experimental data, that the α-helix forms faster than the β-hairpin.},
author = {Irbäck, Anders and Samuelsson, Björn and Sjunnesson, Fredrik and Wallin, Stefan},
issn = {1542-0086},
language = {eng},
number = {3},
pages = {1466--1473},
publisher = {Cell Press},
series = {Biophysical Journal},
title = {Thermodynamics of α- and β-structure formation in proteins},
volume = {85},
year = {2003},
}